Pieris Publication Breustedt, D. A., Korndörfer, I. P., Redl, B. & Skerra, A. (2005) The 1.8-Å; crystal structure of human tear lipocalin reveals an extended branched cavity with capacity for multiple ligands. J. Biol. Chem. 280, 484-493.
Pieris Publication Nygren, P.-Å;. & Skerra, A. (2004) Binding proteins from alternative scaffolds. J. Immunol. Methods 290, 3-28.
Pieris Publication Vogt, M. & Skerra, A. (2004) Construction of an artificial receptor protein (“Anticalin”) based on the human apolipoprotein D. ChemBioChem 5, 191-199.
Pieris Publication Liu, G., Mills, J. L., Hess, T. A., Kim, S., Skalicky, J. J., Sukumaran, D. K., Kupce, E., Skerra, A. & Szyperski, T. (2003) Resonance assignments for the 21 kDa engineered fluorescein-binding lipocalin FluA. J. Biomol. NMR 27, 187-188.
Pieris Publication Korndörfer, I. P., Beste, G. & Skerra, A. (2003) Crystallographic analysis of an “anticalin” with tailored specificity for fluorescein reveals high structural plasticity of the lipocalin loop region. Proteins: Struct. Funct. Genet. 52, 121-129.
Pieris Publication Korndörfer, I. P., Schlehuber, S. & Skerra, A. (2003) Structural mechanism of specific ligand recognition by a lipocalin tailored for the complexation of digoxigenin. J. Mol. Biol. 330, 385-396.
Pieris Publication Götz, M., Hess, S., Beste, G., Skerra, A. & Michel-Beyerle, M.E. (2002) Ultrafast electron transfer in the complex between fluorescein and a cognate engineered lipocalin protein, a so-called anticalin. Biochemistry 41, 4156-4164.
Pieris Publication Schlehuber, S., & Skerra, A. (2002) Tuning ligand affinity, specificity, and folding stability of an engineered lipocalin variant – a so-called ‘anticalin’ – using a molecular random approach. Biophys. Chem. 96, 213-228.
Pieris Publication Skerra, A. (2001) ‘Anticalins’: a new class of engineered ligand-binding proteins with antibody-like properties. Rev. Mol. Biotechnol. 74, 257-275.
Pieris Publication Schlehuber, S., & Skerra, A. (2001) Duocalins: engineered ligand-binding proteins with dual specificity derived from the lipocalin fold. Biol. Chem. 382, 1335-1342.
